Use of conformationally constrained peptides for a topographical analysis of the combing site of a monoclonal anti-substance P antibody.
Biopolymers
; 39(1): 67-74, 1996 Jul.
Article
en En
| MEDLINE
| ID: mdl-8924627
ABSTRACT
The topography of the binding site of a monoclonal anti-substance P antibody directed toward the C-terminal pentapeptide of substance P, Arg-Pro-Lys-Pro-Gln-Gln-Phe-Phe-Gly-Leu-Met-NH2, was analyzed further using a wide range of constrained analogues of substance P. Results obtained in the present study show the following (a) The binding subsites of Phe7 and Phe8 are large and deep, accommodating various side chains, including nonaromatic amino acids. (b) In contrast, the binding pockets for Gly-Leu-Met-NH2 appear more restrictive. Consequently, five residues in the peptide are necessary for the high binding affinity to the antibody, the C-terminal tripeptide determining the binding specificity. These data, which appear to contradict those previously published, illustrate the limits of conclusions drawn from studies generally carried out using exclusively Ala-substituted peptides. In addition, the present results indicate that the topography of the binding site of this monoclonal antibody differs from that of the specific substance P neurokinin-1 receptor, in agreement with the differences observed in the fine specificities of these two substance P binding macromolecules.
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Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Sitios de Unión de Anticuerpos
/
Sustancia P
/
Anticuerpos Monoclonales
Idioma:
En
Revista:
Biopolymers
Año:
1996
Tipo del documento:
Article
País de afiliación:
Francia
Pais de publicación:
EEUU
/
ESTADOS UNIDOS
/
ESTADOS UNIDOS DA AMERICA
/
EUA
/
UNITED STATES
/
UNITED STATES OF AMERICA
/
US
/
USA